Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/4362
Citations
Scopus Web of Science® Altmetric
?
?
Type: Journal article
Title: Caerin 4.1, an antibiotic peptide from the Australian Tree Frog, Litoria caerulea. The N.M.R.-derived solution structure
Author: Chia, C.
Carver, J.
Lindner, R.
Bowie, J.
Wong, H.
Lie, W.
Citation: Australian Journal of Chemistry: an international journal for chemical science, 2000; 53(4):257-265
Publisher: C S I R O Publishing
Issue Date: 2000
ISSN: 0004-9425
Statement of
Responsibility: 
Brian C. S. Chia, John A. Carver, Robyn A. Lindner, John H. Bowie, Herbert Wong and Wilford Lie
Abstract: Caerin 4.1 (GLWQK⁵IKSAA¹⁰GDLAS¹⁵GIEVG²⁰IKS-NH₂) is an antibiotic peptide isolated from the Australian tree frog Litoria caerulea. Unlike caerin 1.1, the major peptide isolated from this species, caerin 4.1 has a narrow spectrum of antibiotic activity, e.g. it shows selective activity against Pasteurella haemolytica and Escherichia coli. Caerin 4.1 consists of 23 amino acid residues and is comparable in size with other wide-spectrum antibiotic peptides isolated from Australian amphibians, e.g. caerin 1.1 and maculatin 1.1. An n.m.r. study in trifluoroethanol/water indicates that caerin 4.1 forms an amphipathic -helix with distinct hydrophilic and hydrophobic zones. Two regions of well defined helicity (from Gln4 to Ala10 and from Ile17 to Ile21) are separated by a central helical region of greater conformational variability. The enhanced disorder in this region arises from the presence of two central glycine residues at positions 11 and 16. However, the degree of disorder and hence flexibility is much less than in caerin 1.1 where central proline residues are present instead. This reduced central flexibility may account for the narrow spectrum of biological activity of caerin 4.1, i.e. because biological membranes of the various bacteria have different composition and topology, their optimal interaction with the relatively rigid caerin 4.1 peptide is not possible.
Description: Copyright © 2000 CSIRO
DOI: 10.1071/CH99108
Published version: http://dx.doi.org/10.1071/ch99108
Appears in Collections:Aurora harvest 6
Chemistry publications

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.